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COPG_ARATH
ID   COPG_ARATH              Reviewed;         886 AA.
AC   Q0WW26; O65673; Q56X38;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Coatomer subunit gamma;
DE   AltName: Full=Gamma-coat protein;
DE            Short=Gamma-COP;
GN   OrderedLocusNames=At4g34450; ORFNames=T4L20.30;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-886.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC       dilysine motifs and reversibly associates with Golgi non-clathrin-
CC       coated vesicles, which further mediate biosynthetic protein transport
CC       from the ER, via the Golgi up to the trans Golgi network. Coatomer
CC       complex is required for budding from Golgi membranes, and is essential
CC       for the retrograde Golgi-to-ER transport of dilysine-tagged proteins
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC       the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC       originating from it. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the COPG family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL023094; CAA18824.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161585; CAB80162.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86378.1; -; Genomic_DNA.
DR   EMBL; AK221839; BAD94079.1; -; mRNA.
DR   EMBL; AK226533; BAE98672.1; -; mRNA.
DR   PIR; T05265; T05265.
DR   RefSeq; NP_195171.2; NM_119610.4.
DR   AlphaFoldDB; Q0WW26; -.
DR   SMR; Q0WW26; -.
DR   BioGRID; 14878; 76.
DR   IntAct; Q0WW26; 1.
DR   STRING; 3702.AT4G34450.1; -.
DR   iPTMnet; Q0WW26; -.
DR   SwissPalm; Q0WW26; -.
DR   PaxDb; Q0WW26; -.
DR   PRIDE; Q0WW26; -.
DR   ProteomicsDB; 240951; -.
DR   EnsemblPlants; AT4G34450.1; AT4G34450.1; AT4G34450.
DR   GeneID; 829596; -.
DR   Gramene; AT4G34450.1; AT4G34450.1; AT4G34450.
DR   KEGG; ath:AT4G34450; -.
DR   Araport; AT4G34450; -.
DR   TAIR; locus:2139479; AT4G34450.
DR   eggNOG; KOG1078; Eukaryota.
DR   HOGENOM; CLU_010353_2_0_1; -.
DR   InParanoid; Q0WW26; -.
DR   OMA; CEGTETI; -.
DR   OrthoDB; 255234at2759; -.
DR   PhylomeDB; Q0WW26; -.
DR   PRO; PR:Q0WW26; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q0WW26; baseline and differential.
DR   Genevisible; Q0WW26; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 2.
DR   Gene3D; 2.60.40.1480; -; 1.
DR   Gene3D; 3.30.310.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR   InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR   InterPro; IPR032154; Coatomer_g_Cpla.
DR   InterPro; IPR017106; Coatomer_gsu.
DR   InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
DR   InterPro; IPR037067; Coatomer_gsu_app_sf.
DR   InterPro; IPR012295; TBP_dom_sf.
DR   PANTHER; PTHR10261; PTHR10261; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF16381; Coatomer_g_Cpla; 1.
DR   Pfam; PF08752; COP-gamma_platf; 1.
DR   PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF49348; SSF49348; 1.
DR   SUPFAM; SSF55711; SSF55711; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..886
FT                   /note="Coatomer subunit gamma"
FT                   /id="PRO_0000285627"
FT   REPEAT          66..103
FT                   /note="HEAT 1"
FT   REPEAT          288..325
FT                   /note="HEAT 2"
FT   REPEAT          327..359
FT                   /note="HEAT 3"
FT   REPEAT          360..397
FT                   /note="HEAT 4"
FT   REPEAT          472..509
FT                   /note="HEAT 5"
FT   REGION          592..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   886 AA;  98491 MW;  188840F332D97CAF CRC64;
     MAQPLVKKDD DHDDELEYSP FMGIEKGAVL QEARVFNDPQ VDPRRCSQVI TKLLYLLNQG
     ESFTKVEATE VFFSVTKLFQ SKDTGLRRMV YLIIKELSPS SDEVIIVTSS LMKDMNSKID
     MYRANAIRVL CRIIDGTLLT QIERYLKQAI VDKNPVVSSA ALVSGLHLLK TNPEIVKRWS
     NEVQEGIQSR SALVQFHALA LLHQIRQNDR LAVSKLVGSL TRGSVRSPLA QCLLIRYTSQ
     VIRDMANHGQ SGERPFYEFL ESCLRHKAEM VILEAARAIT ELDGVTSREL TPAITVLQLF
     LSSPRPVLRF AAVRTLNKVA MTHPMAVTNC NIDMESLISD QNRSIATLAI TTLLKTGNES
     SVERLMKQIT NFMSDIADEF KIVVVDAIRS LCVKFPLKYR SLMTFLSNIL REEGGFEYKR
     AIVDSIVTII RDIPDAKESG LLHLCEFIED CEFTYLSTQI LHFLGIEGPN TSDPSKYIRY
     IYNRVHLENA TVRAAAVSTL AKFGFMVESL KPRITVLLKR CIYDSDDEVR DRATLYLSVL
     GGDGTVDTDK ESKDFLFGSL EVPLVNMETS LKNYEPSEEA FDINSVPKEV KSQPLAEKKA
     QGKKPTGLGA PPAAPASGFD GYERLLSSIP EFAAFGKLFK SSLPVELTEA ETEYAVNVVK
     HIFDSHVVFQ YNCTNTIPEQ LLERVNVIVD ASEAEEFSEV TSKALNSLPY DSPGQAFVVF
     EKPAGVPAVG KFSNTLTFVV KEVDPSTGEA EDDGVEDEYQ LEDLEVVAGD YMVKVGVSNF
     RNAWESMDEE DERVDEYGLG QRESLGEAVK AVMDLLGMQT CEGTETIPLN ARSHTCLLSG
     VYIGNVKVLV RAQFGMDSSK DIAMKLTVRA EDVSVAEAIH EIVASG
 
 
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